Search by BoMiProt ID - Bomi209


Primary Information

BoMiProt ID Bomi209
Protein Name Aspartoacylase
Organism Bos taurus
Uniprot IDP46446
Milk FractionExosome
Aminoacid Length 313
Molecular Weight 35738
FASTA Sequence Download
Gene Name ASPA
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells first partially purified from rat brain and was then subsequently purified to homogeneity from bovine brain; distributed primarily in the oligodendrocytes
Protein Function catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate; the metabolism of NAA appears to be necessary in the formation of myelin lipids, and defects in this enzyme lead to Canavan disease, a fatal neurological disorder. Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspartate to aspartate and acetate in the vertebrate brain.
Biochemical Properties zinc-dependent peptidase; essential metal ion ligands and active-site functional groups of the carboxypeptidases are conserved in the aspartoacylases; Divalent cations are reported to activate the enzyme, but the addition of these cations lead to only modest increases in catalytic activity; not a metalloenzyme
PTMs A putative N-glycosylation site (Asn117) contained in an Asn-X-Thr/Ser recognition sequence; located adjacent to one of the proposed histidine metal ion ligands
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs enzyme activity has been hypothesized to be regulated both by glycosylation and by phosphorylation/dephosphorylation
Additional Comments Mutations that result in near undetectable activity of aspartoacylase, which catalyzes the deacetylation of N-acetyl-l-aspartate, correlate with Canavan Disease, a neurodegenerative disorder usually fatal during childhood.
Bibliography 1. Le Coq, J., An, H.-J., Lebrilla, C., & Viola, R. E. (2006). Characterization of human aspartoacylase: the brain enzyme responsible for Canavan disease. Biochemistry, 45(18), 5878–5884. https://doi.org/10.1021/bi052608w. 2.Hershfield JR, Pattabiraman N, Madhavarao CN, Namboodiri MA. Mutational analysis of aspartoacylase: implications for Canavan disease. Brain Res. 2007 May 7;1148:1-14. doi: 10.1016/j.brainres.2007.02.069. Epub 2007 Mar 3. PMID: 17391648; PMCID: PMC1933483.